Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: human-FASN

Homo sapiens (Human) FAS FASN Fatty acid synthase Thioesterase domain (EC 2.3.1.85)

Comment
previously named human-fas. Only the c-terminal thioesterase module is an alpha/beta hydrolase. Thioesterase is the last module of Fatty acid synthase


Relationship
Family|Thioesterase
Block| X
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
No mutation
6 structures (e.g. : 1XKT, 2PX6, 3TJM... more)
No kinetic





2 substrates: 4-methylumbelliferyl-heptanoate, Orlistat
7 inhibitors (e.g. : AZ12756122, Dihomo-gamma-linolenic-acid, Methyl-gamma-linolenyl-fluorophosphonate... more)
>3 Genbank links 7 more: U26644, S80437, BC063242
1 UniProt : P49327
>3 Structure links 3 more: 7MHD, 7MHE, 4Z49
1 UniProt : P49327
1 Interpro : P49327
1 Prodom : P49327
1 Pfam : P49327
1 PIRSF : P49327
1 SUPERFAM : P49327
1 EntrezGene : 2194
1 SNP : 2194
1 UniGene : 83190
1 HUGO HGNC : 3594
1 IUPHAR : 2608
1 OMIM : 600212
1 Ensembl : ENSG00000169710
Sequence
Graphical view for this peptide sequence: human-FASN
Colored MSA for Thioesterase (raw)
DGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVF
HSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGY
SYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTP
GCEAEPETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKS
HQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGTYGQD
LGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVS
VREG
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

DGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVF
HSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGY
SYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTP
GCEAEPETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKS
HQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGTYGQD
LGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVS
VREG


References
6 more
    Title: Research progress on FASN and MGLL in the regulation of abnormal lipid metabolism and the relationship between tumor invasion and metastasis
    Zhang J, Song Y, Shi Q, Fu L
    Ref: Front Med, :, 2021 : PubMed

            

    Title: Enzyme promiscuity drives branched-chain fatty acid synthesis in adipose tissues
    Wallace M, Green CR, Roberts LS, Lee YM, McCarville JL, Sanchez-Gurmaches J, Meurs N, Gengatharan JM, Hover JD and Metallo CM <7 more author(s)>
    Ref: Nat Chemical Biology, 14:1021, 2018 : PubMed

            

    Title: Estimation of Hydrogen-Exchange Protection Factors from MD Simulation Based on Amide Hydrogen Bonding Analysis
    Park IH, Venable JD, Steckler C, Cellitti SE, Lesley SA, Spraggon G, Brock A
    Ref: J Chem Inf Model, 55:1914, 2015 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer